EPTA_ECOLI
ID EPTA_ECOLI Reviewed; 547 AA.
AC P30845; P76793; Q2M6J0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Phosphoethanolamine transferase EptA;
DE EC=2.7.-.-;
DE AltName: Full=Polymyxin resistance protein PmrC;
GN Name=eptA; Synonyms=pmrC, yjdB; OrderedLocusNames=b4114, JW5730;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 311-547.
RC STRAIN=K12;
RX PubMed=8282725; DOI=10.1093/oxfordjournals.jbchem.a124180;
RA Nagasawa S., Ishige K., Mizuno T.;
RT "Novel members of the two-component signal transduction genes in
RT Escherichia coli.";
RL J. Biochem. 114:350-357(1993).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
CC -!- FUNCTION: Catalyzes the addition of a phosphoethanolamine moiety to the
CC lipid A. The phosphoethanolamine modification is required for
CC resistance to polymyxin. {ECO:0000250|UniProtKB:A0A0H3JML2}.
CC -!- SUBUNIT: Has been isolated as a 91 kDa complex containing ZipA-EptA and
CC an unidentified 24 kDa protein. {ECO:0000269|PubMed:16079137}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16079137}.
CC -!- INDUCTION: The eptA-basRS operon is positively autoregulated by BasR
CC under high iron or aluminum concentration conditions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoethanolamine transferase family. EptA
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97013.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97013.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77075.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78116.1; -; Genomic_DNA.
DR EMBL; D14055; BAA03142.1; -; Genomic_DNA.
DR RefSeq; NP_418538.2; NC_000913.3.
DR RefSeq; WP_000919792.1; NZ_LN832404.1.
DR AlphaFoldDB; P30845; -.
DR SMR; P30845; -.
DR BioGRID; 4263082; 125.
DR DIP; DIP-12561N; -.
DR IntAct; P30845; 2.
DR STRING; 511145.b4114; -.
DR jPOST; P30845; -.
DR PaxDb; P30845; -.
DR PRIDE; P30845; -.
DR EnsemblBacteria; AAC77075; AAC77075; b4114.
DR EnsemblBacteria; BAE78116; BAE78116; BAE78116.
DR GeneID; 948629; -.
DR KEGG; ecj:JW5730; -.
DR KEGG; eco:b4114; -.
DR PATRIC; fig|1411691.4.peg.2586; -.
DR EchoBASE; EB1570; -.
DR eggNOG; COG2194; Bacteria.
DR HOGENOM; CLU_018534_1_0_6; -.
DR InParanoid; P30845; -.
DR OMA; NSIAFYF; -.
DR PhylomeDB; P30845; -.
DR BioCyc; EcoCyc:EG11613-MON; -.
DR BioCyc; MetaCyc:EG11613-MON; -.
DR BRENDA; 2.7.8.43; 2026.
DR PRO; PR:P30845; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IBA:GO_Central.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; TAS:EcoCyc.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012549; EptA-like_N.
DR InterPro; IPR040423; PEA_transferase.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR30443; PTHR30443; 1.
DR Pfam; PF08019; EptA_B_N; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Cell inner membrane; Cell membrane;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..547
FT /note="Phosphoethanolamine transferase EptA"
FT /id="PRO_0000209151"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..47
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..123
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..547
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 547 AA; 61667 MW; AA8CE79DDC2F8D10 CRC64;
MLKRLLKRPS LNLLAWLLLA AFYISICLNI AFFKQVLQAL PLDSLHNVLV FLSMPVVAFS
VINIVLTLSS FLWLNRPLAC LFILVGAAAQ YFIMTYGIVI DRSMIANIID TTPAESYALM
TPQMLLTLGF SGVLAALIAC WIKIKPATSR LRSVLFRGAN ILVSVLLILL VAALFYKDYA
SLFRNNKELV KSLSPSNSIV ASWSWYSHQR LANLPLVRIG EDAHRNPLMQ NEKRKNLTIL
IVGETSRAEN FSLNGYPRET NPRLAKDNVV YFPNTASCGT ATAVSVPCMF SDMPREHYKE
ELAQHQEGVL DIIQRAGINV LWNDNDGGCK GACDRVPHQN VTALNLPDQC INGECYDEVL
FHGLEEYINN LQGDGVIVLH TIGSHGPTYY NRYPPQFRKF TPTCDTNEIQ TCTKEQLVNT
YDNTLVYVDY IVDKAINLLK EHQDKFTTSL VYLSDHGESL GENGIYLHGL PYAIAPDSQK
QVPMLLWLSE DYQKRYQVDQ NCLQKQAQTQ HYSQDNLFST LLGLTGVETK YYQAADDILQ
TCRRVSE
